Impaired processing of human pro-islet amyloid polypeptide is not a causative factor for fibril formation or membrane damage in vitro

Authors :: Khemtemourian, Lucie
Casarramona, Gemma Lahoz
Suylen, Dennis P.L.
Hackeng, Tilman M.
Meeldijk, Johannes D.
de Kruijff, Ben
Hoppener, Jo W.M.
Killian, J. Antoinette
Source :: Biochemistry. Nov 24, 2009, Vol. 48 Issue 46, 10918-10925
Publication Year :: 2009
Abstract: The formation of the amyloid fibrils in solutions by the precursors of the human pro-islet amyloid polypeptide (hIAPP) in humans is discussed. The results demonstrate that the hIAPP precursors play a major role in the prevention of aggregation and membrane change of mature hIAPP and hence are extremely significant.

Subjects :: Catalysis -- Analysis
Diabetes -- Research
Enzyme inhibitors -- Chemical properties
Glycoproteins -- Structure
Glycoproteins -- Chemical properties
Biological sciences
Chemistry

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